Identifying and structurally characterizing CD1b in Aotus nancymaae owl monkeys
| Autor: | Carlos Parra-Lopez, Pilar Martinez, Carlos A. Guerrero, Manuel E. Patarroyo, Luz Mary Salazar, Esperanza Trujillo, Fabio Castillo, Paola Barato, Gabriela Delgado |
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| Rok vydání: | 2004 |
| Předmět: |
Protein Folding
Protein Conformation Structural similarity Molecular Sequence Data Immunology Antigen presentation Receptors Antigen T-Cell Monocytes Conserved sequence Antigens CD1 Mice Protein structure Antigen Genetics Animals Humans Tissue Distribution Amino Acid Sequence Cloning Molecular Peptide sequence Conserved Sequence Aotus nancymaae Antigen Presentation Binding Sites Sequence Homology Amino Acid biology T-cell receptor Dendritic Cells Flow Cytometry biology.organism_classification Molecular biology Cell biology Disease Models Animal Aotidae |
| Zdroj: | Immunogenetics. 56:480-489 |
| ISSN: | 1432-1211 0093-7711 |
| DOI: | 10.1007/s00251-004-0716-8 |
| Popis: | This study reports the molecular characterization and tissue expression of the non-human Aotus nancymaae primate CD1b isoform in the search for an experimental animal model to be used in evaluating the role of non-peptide antigen-presentation molecules in the immune response to infectious agents. CD1b expression on the surface of A. nancymaae peripheral blood monocyte-derived dendritic cells, shown by flow cytometry, was made possible by using human CD1b isoform antibodies. Studying the expression of CD1b-encoded transcripts revealed this molecule's broad distribution in several tissues. The A. nancymaae CD1b transcript-encoded amino-acid sequence showed 95.5% identity with the human sequence. Such high sequence homology was reflected in the identical structural conservation of how pockets A', C' and F' and tunnel T' conforming the antigen's binding site are organized, the similar arrangement of those amino-acids interacting with the T-cell receptor (TCR) during antigen presentation, and the conservation of YQNI-motif sequence in the cytoplasmatic tail (responsible for the molecule's intracellular trafficking in humans). Comparing the structure of human CD1a and CD1b and mouse CD1d proteins with CD1b structure in A. nancymaae obtained by minimization revealed that changes in the latter molecule's alpha1 and alpha2 domains imposed a narrowing of the antigen-binding groove in A. nancymaae CD1b. The high structural similarity between A. nancymaae CD1b and that from humans presented in this study leads to A. nancymaae being proposed as a suitable experimental animal model for analyzing CD1b in vivo, mainly in bacterial and parasite infections such as tuberculosis and malaria, respectively. |
| Databáze: | OpenAIRE |
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